ADAMs are transmembrane proteins containing both a disintegrin (see
<PDOC00351>) and a metalloprotease domain [1]. About two third of the proteins
with an ADAM type metalloprotease domain also contain the zinc protease
pattern (see <PDOC00129>) which locates the active site of these proteases. As
they contain an adhesion domain and a protease domain, ADAM proteins
potentially have both cell adhesion and protease activities. They play a role
in various biological processes, including fertilization, neurogenesis,
myogenesis, embryonic TGF-α release and inflammatory response [2].

ADAMTS proteins [3] form a closely related family of proteases. In these
proteins, the metalloprotease and disintegrin domains are flanked by
thrombospondin type I (TSP1) repeat (see <PDOC50092>). ADAMTS proteins are
soluble, extracellular matrix proteases those known substrates are other
extracellular matrix proteins [2].

ADAM proteins also share the metalloprotease and disintegrin domains with the
disintegrin class of peptides that are present in snake venom [2,4]. Together,
they form the adamlysin/reprolysin subfamily of the metzincin superfamily of
Zn-dependent metalloproteinases [4].

Some proteins known to contain an ADAM metalloprotease domain are listed
below:

Human ADAM 1 and 2 (fertilin α and β). Fertilins are sperm surface
membrane proteins that may be involved in sperm-egg plasma membrane
adhesion and fusion during fertilization. They lack proteolytic activity.

Human ADAM 8. It may be involved in immune function.

Drosophila Kuzbanian. It is involved in neurogenesis. Kuzbanian is a
sheddase that has been found to release a soluble form of Delta, a Notch
ligand.

Vertebrate ADAM 10, the homologue of Kuzbanian.

Caenorhabditis elegans Sup-17, the homologue of Kuzbanian. It is involved
in Lin-12/NOTCH signaling.

Human ADAM 12 (meltrin α). It may be involved in myogenesis.

Several snake venom metalloproteinases of the disintegrin family. They are
not transmembrane proteins.

Mammalian ADAMTS-1. Protease those expression is associated with acute
inflammation as well as development of cancer cachexia.

Last update:

December 2001 / First entry.

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